The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Drugging Topoisomerases: Lessons and Challenges
Open accessAbstract
Topoisomerases are ubiquitous enzymes that control DNA supercoiling and entanglements. They are essential during transcription and replication, and topoisomerase inhibitors are among the most effective and most commonly used anticancer and antibacterial drugs. This review consists of two parts. In the first part ("Lessons"), it gives background information on the catalytic mechanisms of the different enzyme families (6 different genes in humans and 4 in most bacteria), describes the "interfacial inhibition" by which topoisomerase-targeted drugs act as topoisomerase poisons, and describes clinically relevant topoisomerase inhibitors. It generalizes the interfacial inhibition principle, which was discovered from the mechanism of action of topoisomerase inhibitors, and discusses how topoisomerase inhibitors kill cells by trapping topoisomerases on DNA rather than by classical enzymatic inhibition. Trapping protein-DNA complexes extends to a novel mechanism of action of PARP inhibitors and could be applied to the targeting of transcription factors. The second part of the review focuses on the challenges for discovery and precise use of topoisomerase inhibitors, including targeting topoisomerase inhibitors using chemical coupling and encapsulation for selective tumor delivery, use of pharmacodynamic biomarkers to follow drug activity, complexity of the response determinants for anticancer activity and patient selection, prospects of rational combinations with DNA repair inhibitors targeting tyrosyl-DNA-phosphodiesterases 1 and 2 (TDP1 and TDP2) and PARP, and the unmet need to develop inhibitors for type IA enzymes.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The Cancer Cell Line Encyclopedia enables predictive modelling of anticancer drug sensitivity
Barretina, J., Caponigro, G., Stransky, N., Venkatesan, K., Margolin, A. A., Kim, S., Wilson, C. J., Lehár, J., Kryukov, G. V., Sonkin, D., et al. (2012) · Nature · doi:10.1038/nature11003 · Cited by 7,950
Systematic identification of genomic markers of drug sensitivity in cancer cells
Garnett, M. J., Edelman, E. J., Heidorn, S. J., Greenman, C. D., Dastur, A., Lau, K. W., Greninger, P., Thompson, I. R., Luo, X., Soares, J., et al. (2012) · Nature · doi:10.1038/nature11005 · Cited by 2,456
Tewey, K. M., Chen, G. L., Nelson, E. M., & Liu, L. F. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)47282-6 · Cited by 887
Takashima, H., Boerkoel, C. F., John, J., Saifi, G. M., Salih, M. A. M., Armstrong, D., Mao, Y., Quiocho, F. A., Roa, B. B., Nakagawa, M., et al. (2002) · Nature Genetics · doi:10.1038/ng987 · Cited by 522
Cited by
Rad51-mediated replication fork reversal is a global response to genotoxic treatments in human cells
Zellweger, R., Dalcher, D., Mutreja, K., Berti, M., Schmid, J. A., Herrador, R., Vindigni, A., & Lopes, M. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201406099 · Cited by 677
Topoisomerases as anticancer targets
Delgado, J. L., Hsieh, C.-M., Chan, N.-L., & Hiasa, H. (2018) · Biochemical Journal · doi:10.1042/bcj20160583 · Cited by 481
Topoisomerases facilitate transcription of long genes linked to autism
King, I. F., Yandava, C. N., Mabb, A. M., Hsiao, J. S., Huang, H.-S., Pearson, B. L., Calabrese, J. M., Starmer, J., Parker, J. S., Magnuson, T., et al. (2013) · Nature · doi:10.1038/nature12504 · Cited by 438
Cai, K., He, X., Song, Z., Yin, Q., Zhang, Y., Uckun, F. M., Jiang, C., & Cheng, J. (2015) · Journal of the American Chemical Society · doi:10.1021/ja513034e · Cited by 363
DNA double-strand break repair pathway choice and cancer
Aparicio, T., Baer, R., & Gautier, J. (2014) · DNA Repair · doi:10.1016/j.dnarep.2014.03.014 · Cited by 347
Exploiting replicative stress to treat cancer
Dobbelstein, M., & Sørensen, C. S. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4553 · Cited by 302
Murai, J., Zhang, Y., Morris, J., Ji, J., Takeda, S., Doroshow, J. H., & Pommier, Y. (2014) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.113.210146 · Cited by 293
Self-citationIrinotecan—Still an Important Player in Cancer Chemotherapy: A Comprehensive Overview
Kciuk, M., Marciniak, B., & Kontek, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144919 · Cited by 266
Anthracyclines as Topoisomerase II Poisons: From Early Studies to New Perspectives
Marinello, J., Delcuratolo, M., & Capranico, G. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113480 · Cited by 258
Payload diversification: a key step in the development of antibody–drug conjugates
Conilh, L., Sadilkova, L., Viricel, W., & Dumontet, C. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01397-y · Cited by 257
cGAS/STING axis mediates a topoisomerase II inhibitor–induced tumor immunogenicity
Wang, Z., Chen, J., Hu, J., Zhang, H., Xu, F., He, W., Wang, X., Li, M., Lu, W., Zeng, G., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci127471 · Cited by 253
Trapping Poly(ADP-Ribose) Polymerase
Shen, Y., Aoyagi-Scharber, M., & Wang, B. (2015) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.222448 · Cited by 230
Murai, J., Thomas, A., Miettinen, M., & Pommier, Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.05.009 · Cited by 172
Self-citationTheory and Applications of Covalent Docking in Drug Discovery: Merits and Pitfalls
Kumalo, H., Bhakat, S., & Soliman, M. (2015) · Molecules · doi:10.3390/molecules20021984 · Cited by 158
Naphthoquinones: A continuing source for discovery of therapeutic antineoplastic agents
Qiu, H., Wang, P., Lin, H., Tang, C., Zhu, H., & Yang, Y. (2018) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13141 · Cited by 118
Targeting DNA Replication Stress for Cancer Therapy
Zhang, J., Dai, Q., Park, D., & Deng, X. (2016) · Genes · doi:10.3390/genes7080051 · Cited by 102
Trellis tree-based analysis reveals stromal regulation of patient-derived organoid drug responses
Ramos Zapatero, M., Tong, A., Opzoomer, J. W., O’Sullivan, R., Cardoso Rodriguez, F., Sufi, J., Vlckova, P., Nattress, C., Qin, X., Claus, J., et al. (2023) · Cell · doi:10.1016/j.cell.2023.11.005 · Cited by 72
Autophagy Regulation on Cancer Stem Cell Maintenance, Metastasis, and Therapy Resistance
Wang, X., Lee, J., & Xie, C. (2022) · Cancers · doi:10.3390/cancers14020381 · Cited by 53
Roberts, J. A., Varma, V. R., An, Y., Varma, S., Candia, J., Fantoni, G., Tiwari, V., Anerillas, C., Williamson, A., Saito, A., et al. (2021) · Science Advances · doi:10.1126/sciadv.abi8178 · Cited by 49
Detection of topoisomerase covalent complexes in eukaryotic cells
Anand, J., Sun, Y., Zhao, Y., Nitiss, K. C., & Nitiss, J. L. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7459-7_20 · Cited by 31
Jeon, K.-H., Park, S., Shin, J.-H., Jung, A.-R., Hwang, S.-Y., Seo, S. H., Jo, H., Na, Y., & Kwon, Y. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114999 · Cited by 9
Metadata
- Authors
- Pommier, Y.
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2013-01-04
- Volume
- 8
- Issue
- 1
- Pages
- 82-95
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- OpenAlex
- W2014014132
- Cited by
- 839
- References
- 4
- FWCI
- 18.59
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
